2014
Characterization of Unfolding Mechanism of Human Lamin A Ig Fold by Single-Molecule Force SpectroscopyImplications in EDMD
Bera M, Kotamarthi H, Dutta S, Ray A, Ghosh S, Bhattacharyya D, Ainavarapu S, Sengupta K. Characterization of Unfolding Mechanism of Human Lamin A Ig Fold by Single-Molecule Force SpectroscopyImplications in EDMD. Biochemistry 2014, 53: 7247-7258. PMID: 25343322, DOI: 10.1021/bi500726f.Peer-Reviewed Original ResearchConceptsIg domainsBasic nuclear processesB-type laminsC-terminal domainHelical rod domainAutosomal dominant Emery-Dreifuss muscular dystrophySingle-molecule force spectroscopyEmery-Dreifuss muscular dystrophyIntermediate filament proteinsHuman laminLamin proteinsNuclear laminaLamin ALamin A.Nuclear envelopeRod domainNuclear processesUnfolding mechanismFilament proteinsMisshapen nucleiCausative mutationsKey playersR453WLaminsMutations
1987
A new lamin in Xenopus somatic tissues displays strong homology to human lamin A.
Wolin S, Krohne G, Kirschner M. A new lamin in Xenopus somatic tissues displays strong homology to human lamin A. The EMBO Journal 1987, 6: 3809-3818. PMID: 3428277, PMCID: PMC553853, DOI: 10.1002/j.1460-2075.1987.tb02717.x.Peer-Reviewed Original ResearchConceptsHuman lamin ACDNA clonesXenopus laminSomatic tissuesLamin AMajor lamin proteinsCarboxy-terminal domainAdult somatic cellsHuman lamin A.Major laminsDistinct structural classesLamin proteinsNuclear laminaLamin LIIIEmbryonic developmentSomatic cellsSomatic laminsStrong homologyLamin A.Lamin LILaminsMajor polypeptidesGerm cellsProteinClones
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply